Journal
MACROMOLECULAR BIOSCIENCE
Volume 22, Issue 2, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/mabi.202100299
Keywords
antibody-inspired conjugates; avidin-biotin; boronic acid-salicylhydroxamate; pH-responsive linkers; protein-drug conjugates
Funding
- Max Planck Society
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [SFB 1066, 213555243]
- DFG Emmy Noether Program [417278389]
- Projekt DEAL
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By combining a supramolecular protein-based assembly platform and a pH-responsive linker, the authors have devised a convenient assembly of a trivalent protein-drug conjugate that possesses distinct features of ADCs. These ADC-like conjugates target cancer cells that overexpress somatostatin receptors, enable controlled release in the cancer cell microenvironment through a new pH-responsive biotin linker, and exhibit stability in biological media.
With the advent of chemical strategies that allow the design of smart bioconjugates, peptide- and protein-drug conjugates are emerging as highly efficient therapeutics to overcome limitations of conventional treatment, as exemplified by antibody-drug conjugates (ADCs). While targeting peptides serve similar roles as antibodies to recognize overexpressed receptors on diseased cell surfaces, peptide-drug conjugates suffer from poor stability and bioavailability due to their low molecular weights. Through a combination of a supramolecular protein-based assembly platform and a pH-responsive linker, the authors devise herein the convenient assembly of a trivalent protein-drug conjugate. The conjugate should ideally possess distinct features of ADCs such as 1) recognition sites that recognize cell receptor and are arranged on 2) distinct locations on a high molecular weight protein scaffold, 3) a stimuli-responsive linker, as well as 4) an attached payload such as a drug molecule. These AD-like conjugates target cancer cells that overexpress somatostatin receptors, can enable controlled release in the microenvironment of cancer cells through a new pH-responsive biotin linker, and exhibit stability in biological media.
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